Deduced Amino Acid Sequence of the Fusion Glycoprotein of Turkey Rhinotracheitis Virus has Greater Identity with that of Human Respiratory Syncytial Virus, a Pneumovirus, than that of Paramyxoviruses and Morbilliviruses

1 Institute for Animal Health, Division of Molecular Biology, Houghton Laboratory, Houghton, Huntingdon, Cambridgeshire PE17 2DA and 2 Pirbright Laboratory, Pirbright, Woking, Surrey GU24 0NF, U.K. The sequence of the fusion (F) glycoprotein of turkey rhinotracheitis virus (TRTV) has been deduced fr...

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Published inJournal of general virology Vol. 72; no. 1; pp. 75 - 81
Main Authors Yu, Q, Davis, P. J, Barrett, T, Binns, M. M, Boursnell, M. E. G, Cavanagh, D
Format Journal Article
LanguageEnglish
Published Reading Soc General Microbiol 01.01.1991
Society for General Microbiology
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Summary:1 Institute for Animal Health, Division of Molecular Biology, Houghton Laboratory, Houghton, Huntingdon, Cambridgeshire PE17 2DA and 2 Pirbright Laboratory, Pirbright, Woking, Surrey GU24 0NF, U.K. The sequence of the fusion (F) glycoprotein of turkey rhinotracheitis virus (TRTV) has been deduced from cDNA clones derived from oligo(dT)-selected infected cell RNA. The protein consists of 538 amino acids, the F2 and F1 subunits containing 102 (including the F2-F1 connecting peptide RRRR) and 436 residues, respectively. Each subunit has one potential N -linked glycosylation site. The protein has 38 to 39% amino acid identity with the F protein of respiratory syncytial virus ( Pneumovirus genus) but only about half that with members of the other two genera ( Paramyxovirus and Morbillivirus ) in the Paramyxoviridae family. This is the first sequence evidence to support the view that TRTV is a pneumovirus, the first avian member of the genus to be described. Present address: Animal Health Trust, Lanwades Park, Kennett, Newmarket, Suffolk CB8 7PN, U.K. > Present address: Immunology Limited, 184 Cambridge Science Park, Milton Road, Cambridge CB4 4GN, U.K. Received 24 August 1990; accepted 12 October 1990.
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ISSN:0022-1317
1465-2099
DOI:10.1099/0022-1317-72-1-75